CTTB2_COLGU
ID CTTB2_COLGU Reviewed; 1663 AA.
AC Q07DY4;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 56.
DE RecName: Full=Cortactin-binding protein 2;
DE Short=CortBP2;
GN Name=CTTNBP2; Synonyms=CORTBP2;
OS Colobus guereza (Mantled guereza) (Eastern black-and-white colobus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Colobinae; Colobus.
OX NCBI_TaxID=33548;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Antonellis A., Ayele K., Benjamin B., Blakesley R.W., Boakye A.,
RA Bouffard G.G., Brinkley C., Brooks S., Chu G., Coleman H., Engle J.,
RA Gestole M., Greene A., Guan X., Gupta J., Haghighi P., Han J., Hansen N.,
RA Ho S.-L., Hu P., Hunter G., Hurle B., Idol J.R., Kwong P., Laric P.,
RA Larson S., Lee-Lin S.-Q., Legaspi R., Madden M., Maduro Q.L., Maduro V.B.,
RA Margulies E.H., Masiello C., Maskeri B., McDowell J., Mojidi H.A.,
RA Mullikin J.C., Oestreicher J.S., Park M., Portnoy M.E., Prasad A., Puri O.,
RA Reddix-Dugue N., Schandler K., Schueler M.G., Sison C., Stantripop S.,
RA Stephen E., Taye A., Thomas J.W., Thomas P.J., Tsipouri V., Ung L.,
RA Vogt J.L., Wetherby K.D., Young A., Green E.D.;
RT "NISC comparative sequencing initiative.";
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Regulates the dendritic spine distribution of CTTN/cortactin
CC in hippocampal neurons, thus controls dendritic spinogenesis and
CC dendritic spine maintenance. {ECO:0000250}.
CC -!- SUBUNIT: Interacts with CTTN/cortactin SH3 domain. Interacts with STRN,
CC STRN4/zinedin and MOB4/phocein; this interaction may regulate dendritic
CC spine distribution of STRN and STRN4 in hippocampal neurons. Activation
CC of glutamate receptors weakens the interaction with STRN and STRN4.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cell cortex {ECO:0000250}. Cell
CC projection, dendritic spine {ECO:0000250}. Note=Remains associated with
CC dendritic spines even after glutamate stimulation. {ECO:0000250}.
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DR EMBL; DP000193; ABJ08858.1; -; Genomic_DNA.
DR AlphaFoldDB; Q07DY4; -.
DR SMR; Q07DY4; -.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR GO; GO:0043197; C:dendritic spine; IEA:UniProtKB-SubCell.
DR Gene3D; 1.25.40.20; -; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR019131; Cortactin-binding_p2_N.
DR Pfam; PF12796; Ank_2; 2.
DR Pfam; PF09727; CortBP2; 2.
DR SMART; SM00248; ANK; 6.
DR SUPFAM; SSF48403; SSF48403; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 4.
PE 3: Inferred from homology;
KW ANK repeat; Cell projection; Coiled coil; Cytoplasm; Methylation;
KW Phosphoprotein; Repeat; Synapse.
FT CHAIN 1..1663
FT /note="Cortactin-binding protein 2"
FT /id="PRO_0000260403"
FT REPEAT 709..739
FT /note="ANK 1"
FT REPEAT 743..772
FT /note="ANK 2"
FT REPEAT 776..805
FT /note="ANK 3"
FT REPEAT 809..838
FT /note="ANK 4"
FT REPEAT 842..871
FT /note="ANK 5"
FT REPEAT 912..942
FT /note="ANK 6"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 203..222
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 358..440
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 454..479
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 499..616
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1446..1477
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1580..1602
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1618..1663
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 119..276
FT /evidence="ECO:0000255"
FT COMPBIAS 393..407
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 408..427
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 455..479
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 540..557
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 567..607
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1618..1646
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1647..1663
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 498
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:B9EJA2"
FT MOD_RES 1524
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WZ74"
SQ SEQUENCE 1663 AA; 181225 MW; 26ED232CDA462AE4 CRC64;
MATDGASCEP DLSRAPEDAA GAAAEAAKKE FDVDTLSKSE LRMLLSVMEG ELEARDLVIE
ALRARRKEVF IQERYGRFNL NDPFLALQRD YEAGAGDKEK KPVCTNPLSI LEAVMAHCKK
MQERMSAQLA AAESRQKKLE MEKLQLQALE QEHKKLAARL EEERGKNKQV VLMLVKECKQ
LSGKVIEEAQ KLEDIMAKLE EEKKKTNELE EELSAEKRRS TEMEAQMEKQ LSEFDTEREQ
LRAKLNREEA HTTDLKEEID KMKKMIEQLK RGSDSKPSLS LPRKTKDRRL VSISVGTEGT
VTRSVACQTD LVTESADHVK KLPLTMPVKP STGSPLVSAN AKGSVCTSAT MARPGIDRQA
SHGDLIGSSV PAFPPPSANR IEENGPSTDS TPDPTSSTPP LPSNAAPPTT QTPGIAPQNS
QAPPMHSLHS PCANASLHPG LNPRIQAARF RFQGNANDPD QNGNTTQSPP SRDMSPTSRE
NLVAKQLARN TVTQALSRFT SPQAGAPSRP GAPPTGDVGT HPPVGRTSLK THGVARVDRG
NPPPIPPKKP GLSQTPSPPH PQLKVIIDSS RASNTGAKVD NKTVASPPSS LPQGNRVINE
DNLPKSSSPQ LPPKPSIDLT VAPAGCAVSA LATSQVGAWP AATPGLNQPA CSDSSLVIPT
TIAFCSSINP VSASSCRPGA SDSLLVTASG WSPSLTPLLM SGGPAPLAGR PTLLQQAAAQ
GNVTLLSMLL NEEGLDINYS CEDGHSALYS AAKNGHTDCV RLLLSAEAQI NAADKNGFTP
LCAAAAQGHF ECVELLIAYD ANINHAADGG QTPLYLACKN ENKECIKLLL EAGTNRSVKT
TDGWTPVHAA VDTGNVDSLK LLMYHRIPAC GNSFNEEESE SGVFDLDGGE ESPEGIFKPV
VPADLINHAN REGWTAAHIA ASKGFKNCLE ILCRHGGLEP ERRDKCNRTV HDVATDDCKH
LLENLNALKI PLRISVGEIE PSDYGSDDLE CENTICALNI RKQTSWDDFS KAVSQALTNH
FQAISSDGWW SLEDVTCNNT TDSNIGLSAR SIRSITLGNV PWSVGQSFTQ SPWDFMRKNK
AEHITVLLSG PQEGCLSSVT YASMIPLQMM QNYLRLVEQY HNVIFHGPEG SLQDYIVHQL
ALCLKHRQMA AGFSCEIVRA EIDAGFSKEQ LLDLFISSAC LIPVKQSPSK KKIIIILENL
EKSSLSELLR DFLAPLENRS TESPCTFQKG NGMSECYYFH ENCFLMGTIA KACLQGSDLL
VQQHFRWVQL RWDGEPMQGL LQRFLRRKVV NKFKGQAPSP CDPVCKIVDW ALSVWRQLNS
CLARLGTPEA LLGPKYFLSC PVVPGHAQVT VKWMSKLWNG VIAPRVQEAI LSRASVKRQP
GFGQTTAKRH PSQGQQAVVK AALSILLNKA VLHGCPLPRA ELDQHTADFK GGSFPLSIVS
SYNSCNKKKG ESGAWRKVNT SPRRKSGRFS LPTWNKPDLS TEGIKNKTIS QLNYNRNASL
SKQKSLENDL SLTLNLDQRL SLGSDDEADL VKELQSMCSS KSESDISKIA DSRDDLRMFD
SSGNNPLLSA TINNLRMPVS QKEVSPLSSH QTTECSNSKS KTELGVSRVK SFLPVPRSKV
TLCSQNTKRS SSSSNTRQIE INNNSKKENW NLHKNEHLDK PNK